The structure of an N-terminal fragment of CD4 has been determined to 2.4 Å resolution. It has two tightly abutting domains connected by a continuous β strand. Both have the immunoglobulin fold, but domain 2 has a truncated β barrel and a non-standard disulphide bond. The binding sites for monoclonal antibodies, class II major histocom-patibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
|Number of pages||8|
|State||Published - 1990|
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